2ZAK

Orthorhombic crystal structure of precursor E. coli isoaspartyl peptidase/L-asparaginase (EcAIII) with active-site T179A mutation

Summary for 2ZAK

• Entry DOI: 10.2210/pdb2zak/pdb
• Related: 1JN9 1K2X 1P4V 1SEO 1T3M 2GAC 2GEZ 9GAA 9GAC 9GAF
• Descriptor: L-asparaginase precursor, SODIUM ION, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: isoaspartyl peptidase, asparaginase, ntn-hydrolase, autoproteolysis, precursor, hydrolase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 66764.38

Authors

Michalska, K.,Hernandez-Santoyo, A.,Jaskolski, M. (deposition date: 2007-10-07, release date: 2008-03-25, Last modification date: 2023-11-01)

Primary citation

Michalska, K.,Borek, D.,Hernandez-Santoyo, A.,Jaskolski, M.
Crystal packing of plant-type L-asparaginase from Escherichia coli
Acta Crystallogr.,Sect.D, 64:309-320, 2008

PubMed Abstract: Plant-type L-asparaginases hydrolyze the side-chain amide bond of L-asparagine or its beta-peptides. They belong to the N-terminal nucleophile (Ntn) hydrolases and are synthesized as inactive precursor molecules. Activation occurs via the autoproteolytic release of two subunits, alpha and beta, the latter of which carries the nucleophile at its N-terminus. Crystallographic studies of plant-type asparaginases have focused on an Escherichia coli homologue (EcAIII), which has been crystallized in several crystal forms. Although they all belong to the same P2 1 2 1 2 1 space group with similar unit-cell parameters, they display different crystal-packing arrangements and thus should be classified as separate polymorphs. This variability stems mainly from different positions of the EcAIII molecules within the unit cell, although they also exhibit slight differences in orientation. The intermolecular interactions that trigger different crystal lattice formation are mediated by ions, which represent the most variable component of the crystallization conditions. This behaviour confirms recent observations that small molecules might promote protein crystal lattice formation.

PubMed: 18323626
DOI: 10.1107/S0907444907068072

Experimental method

X-RAY DIFFRACTION (2.01 Å)